Properties of the Endolytic Transglycosylase Encoded by Gene 144 of Pseudomonas aeruginosa Bacteriophage phiKZ

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K. A. Miroshnikov^*, N. M. Faizullina, N. N. Sykilinda, and V. V. Mesyanzhinov

Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; fax: (7-495) 335-0812; E-mail: root@mail.ibch.ru; www.ibch.ru; kmi@ibch.ru

^* To whom correspondence should be addressed.

Received December 16, 2004; Revision received April 13, 2005

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Bacteriophage endolysins degrading bacterial cell walls are prospective enzymes for therapy of bacterial infections. The genome of the giant bacteriophage phiKZ of Pseudomonas aeruginosa encodes two endolysins, gene products (g.p.) 144 and 181, which are homologous to lytic transglycosylases. Gene 144 encoding a 260 amino acid residue protein was cloned into the plasmid expression vector. Recombinant g.p. 144 purified from Escherichia coli effectively degrades chloroform-treated P. aeruginosa cell walls. The protein has predominantly alpha-helical conformation and exists in solution in stoichiometric monomer : dimer : trimer equilibrium. Antibodies against the protein bind the phage particle. This demonstrates that g.p. 144 is a structural component of the phiKZ particle, presumably, a phage tail.

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KEY WORDS: Pseudomonas aeruginosa, bacteriophage phiKZ, endolysin, enzybiotic

DOI: 10.1134/S0006297906030102

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